5FPQ
Structure of Homo sapiens acetylcholinesterase phosphonylated by sarin.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 104.869, 104.869, 323.250 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 45.410 - 2.400 |
| R-factor | 0.1784 |
| Rwork | 0.177 |
| R-free | 0.21030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ey4 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.081 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | REFMAC |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.200 | |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.100 | 0.460 |
| Number of reflections | 81717 | |
| <I/σ(I)> | 11.2 | 3.9 |
| Completeness [%] | 99.6 | 99.4 |
| Redundancy | 5 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | PH 7 |
